ID A0A670K5C0_PODMU Unreviewed; 2298 AA.
AC A0A670K5C0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=Cullin 9 {ECO:0008006|Google:ProtNLM};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000032723.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000032723.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000032723.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSPMRT00000034699.1; ENSPMRP00000032723.1; ENSPMRG00000021181.1.
DR GeneTree; ENSGT00940000153954; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000472272; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR CDD; cd16624; RING-HC_RBR_CUL9; 1.
DR FunFam; 2.60.120.260:FF:000046; Cullin 9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.230.130; Cullin, Chain C, Domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR056405; ARM_CUL7_CUL9.
DR InterPro; IPR047561; BRcat_RBR_CUL9.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR055486; CUL7/CUL9_N.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047560; Rcat_RBR_CUL9.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR047562; RING-HC_RBR_CUL9.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771:SF4; CULLIN 7-RELATED; 1.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF24742; ARM_CUL7_CUL9; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF23168; CUL7_CUL9_N; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472272};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 988..1167
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1378..1641
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 1875..2092
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1879..1926
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 2045..2088
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 604..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2164..2212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 613..624
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2298 AA; 259555 MW; BDA99B5768592BA1 CRC64;
MVGERRNGNL LVHLGPKLQA YPEELIRQRR GHDGHTEYLI RWSILSLDDS LGNSANAASS
ESKTENILMW MSAEEVYANC PTLLGKRKPE GQRVKEEKAP STYPSDVTLD EASLLEMKAD
VRNLVQRAAR QMARTTGPES SILNTIHVLS AYASIGSLTG VFKETGALDL LMKMLCNEEK
QIRRSAGKML RALASHDAGS RAYVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC
MSFEGIHLPQ IPGKLLFSLV KRYLCVTSLM DKLNSTTELG GERQDCAAPS ANFGEKSRVQ
REFDFSMAMA NLISELVRVM GWDRSQEREL SLRETQPRVV RSIFQPKGST CTAVQVPLVT
PKPSPRKKQG QGFLTLSDFS NRSSYVEYVQ ENLKPGMTVR MLEDYEEINI GDEGEFRQSN
SGMPPVQVLW QSTGRTYWVH WHMIEITGSG DSSQAAFCFL SLHAVTKTFY CKPLGGLYSL
PYLTDRMNEN SGTLSRAEWW ELLFFIKKLE QQEQQEVVQF IQQNHEEVSE LDEEGLIQLS
VSVELAKKVL QLLSKYCQGC TCSDLHSSHI YLKYSFSKGG TEQNCQNADV TPLDCGGLSE
GMASKMPKKE SLSAEVPSPA PSAAEKTDTQ LINELLKVEG LSFPDTLDEK AKSKCARQHP
HLRSFGVTGK RNSLEKLTDV VDIIQKSSSE VALQMAGLRF ITKILEDEPG QERQTPVGYN
RGLLVVLREK MVKMLVELLS NQVKEKLLVV MALRLLYVFM AKYDWRVLFA TEGGVRAVLG
CMQEYPASAL VQQAGLAALK VLVGAGNCEL LGSGGKANPL NHSDAQMMRE IFASIGSASG
KDSDNLLCVI CTAIEKMLGT PGILNKFLDS TQEDALPWHE CIEPCLSSLS ANSNDREVVQ
EFIRFLHRLA TTNKDCAVVM SRVGTKEALT KAMDRYNSNL LLVTELRDLV TDCEKYASLY
KKMTTSILAG CIQMVLGQIE EHRRSHQPIN IPFFDVFLRN LCQGSNVEVK EDKCWERVEV
SSNPHRASKL TDRNPKTYWE SNGSTGSHYI NVYMHRGVVV RQMTLLVASE DSSYMPARIV
VMGGENSSNI TTELITLNVL PSASRVVLLE NMARFWPIIQ IKIKRCQQGG IDTRVRGIEV
LGPKPTFWPI FKEQLCRRTY LFYTTKAHTW SADPPPLCPF RLNSALRHEQ VFADRFLPDD
EAAQALGKTC WEALISPLVQ SITTPDPSGI SPLSWLLSQY LENLEASRSA KSRAAIFNSR
VRRLSHLLVH VDSSSPEAEE LKPPVKSSDS GTVKAAVKKP SSTTGITQCW KGVVQQQVKL
FLESSWQAPD FVERYCNTYL RLRTAMEELF GQQMSFMLAL CHGFSGGLLQ LSFLTAMHVS
EQFARYIDRW IQESWADSGN VETLRRLQQS LEPVLFLAGL ELANTFEHFY RYYMGDRLLS
QGKTWLECAV VEHIGLCFPN RFPQQMLKNL SELEEQQQQF HLFQLEQLDK HLLELDQDGN
WEAEEEMEEG EVRDKGQLFS REEEAEVKVL ALSPRCWTIS SFCYLEDPAR FFPESLSQHL
SKFADFYTQS ECQAVLEPNP RRLQWTWLGH AELEYQGCLL HVSTLQMYIL LCFNTEVSVD
TLLQATDLSP VLLHHALKPL TNENGILTQS QNVLRLNEGR LSQMSGQRLW LLPKQTYLNV
EENEGSALER KRNIICCLLI QILKEEKEIH IDNLVFKVWD AGTGPCSAVR LVGEAFCCSS
TDVLSCILHL LSQGYILRQE ENPQLLEYIC AEPTTPHRGQ AQLDAFGLGT EQVLMETVLL
PMGRTMSQDE VEVLMNQTVQ RVSDTLSVTA DVAQHLLIHC KWNVDVLIQR YTEDPEVLLF
SSGMQVRNPQ EPSSPVTHCP VCVNLLSQDD NPPVLCCMHY CCKSCWNEYL TTRIEQNLIL
NCTCPISDCP AQPTTAFIRS IISSKEVIAK YEKALLRGYV ECCSNLTWCT NPQGCDQILC
KEGLGCGEAC SKCSWISCFN CNFPEAHYPA SCSHMSQWMD DGGFYEGMTV EAQSKHLAKL
ISKRCPSCQA QIEKNEGCLH MTCAKCNHGF CWRCLKPWKP THKDYYNCSA MVSKAARQEK
RFQDYNERCT FHHQAREFAM NLRNRVSTVS DVPQIRSLTF VVDTCKMLEQ ARKVLAYSCV
YSYYNQDTEK IDIMEQQSEN LELHTNALQI LLEEMLLQCQ DLASSIRLLK AEHFNTGLEL
VRRIQERLLA ILQHATQDFR VGFQTRQGSE QREMKLSNVP NQACSELDTI FGSFSNNSLS
KNHMLSISSR FSIVSPRG
//
